NMDA1_DROYA
ID NMDA1_DROYA Reviewed; 997 AA.
AC B4PVB0;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Glutamate [NMDA] receptor subunit 1 {ECO:0000250|UniProtKB:Q24418};
DE Flags: Precursor;
GN Name=Nmdar1 {ECO:0000250|UniProtKB:Q24418}; ORFNames=GE25274;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1] {ECO:0000312|EMBL:EDW95779.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01 {ECO:0000312|EMBL:EDW95779.1};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: NMDA receptor subtype of glutamate-gated ion channels with
CC high calcium permeability and voltage-dependent sensitivity to
CC magnesium. Mediated by glycine. This protein plays a key role in
CC synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition
CC and learning. It mediates neuronal functions in glutamate
CC neurotransmission. Is involved in the cell surface targeting of NMDA
CC receptors. Plays a role in associative learning and in long-term memory
CC consolidation (By similarity). {ECO:0000250|UniProtKB:P35439,
CC ECO:0000250|UniProtKB:Q24418}.
CC -!- SUBUNIT: Forms a heteromeric NMDA channel with Nmdar2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q24418};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q24418}.
CC Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q24418}. Postsynaptic
CC density {ECO:0000250|UniProtKB:Q24418}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. {ECO:0000305}.
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DR EMBL; CM000160; EDW95779.1; -; Genomic_DNA.
DR RefSeq; XP_002096067.1; XM_002096031.2.
DR RefSeq; XP_015047145.1; XM_015191659.1.
DR RefSeq; XP_015047146.1; XM_015191660.1.
DR AlphaFoldDB; B4PVB0; -.
DR SMR; B4PVB0; -.
DR STRING; 7245.FBpp0270284; -.
DR EnsemblMetazoa; FBtr0271792; FBpp0270284; FBgn0242356.
DR EnsemblMetazoa; FBtr0399570; FBpp0358592; FBgn0242356.
DR EnsemblMetazoa; FBtr0406016; FBpp0364617; FBgn0242356.
DR GeneID; 6535418; -.
DR KEGG; dya:Dyak_GE25274; -.
DR eggNOG; KOG4440; Eukaryota.
DR HOGENOM; CLU_007257_2_0_1; -.
DR OMA; KPEGFMI; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; B4PVB0; -.
DR Proteomes; UP000002282; Chromosome 3R.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0017146; C:NMDA selective glutamate receptor complex; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; ISS:UniProtKB.
DR GO; GO:0055074; P:calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; ISS:UniProtKB.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007616; P:long-term memory; ISS:UniProtKB.
DR GO; GO:0008355; P:olfactory learning; ISS:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; ISS:UniProtKB.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR018882; CaM-bd_C0_NMDA_rcpt_NR1.
DR InterPro; IPR019594; Glu/Gly-bd.
DR InterPro; IPR001508; Iono_rcpt_met.
DR InterPro; IPR001320; Iontro_rcpt.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF01094; ANF_receptor; 2.
DR Pfam; PF10562; CaM_bdg_C0; 1.
DR Pfam; PF00060; Lig_chan; 1.
DR Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR PRINTS; PR00177; NMDARECEPTOR.
DR SMART; SM00918; Lig_chan-Glu_bd; 1.
DR SMART; SM00079; PBPe; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 3: Inferred from homology;
KW Calcium; Cell membrane; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; Ligand-gated ion channel; Magnesium; Membrane;
KW Phosphoprotein; Postsynaptic cell membrane; Receptor; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..997
FT /note="Glutamate [NMDA] receptor subunit 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000364004"
FT TOPO_DOM 27..573
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 574..594
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 595..651
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 652..672
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 673..831
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 832..852
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 853..997
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 970..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 530..532
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT BINDING 537
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT BINDING 703
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT BINDING 747
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 693
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 93
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q05586"
SQ SEQUENCE 997 AA; 112181 MW; 2462C46A28A3FDD4 CRC64;
MAVAGFVFCW PLLGLTIVLL VAPIDAAQRH TASDNPSTYN IGGVLSNSDS EEHFSTTIKH
LNFDQQYVPR KVTYYDKTIR MDKNPIKTVF NVCDKLIENR VYAVVVSHEQ TSGDLSPAAV
SYTSGFYSIP VIGISSRDAA FSDKNIHVSF LRTVPPYYHQ ADVWLEMLSH FAYTKVIIIH
SSDTDGRAIL GRFQTTSQTY YDDVDVRATV ELIVEFEPKL ESFTEHLIDM KTAQSRVYLM
YASTEDAQVI FRDAGEYNMT GEGHVWIVTE QALFSNNTPD GVLGLQLEHA HSDKGHIRDS
VYVLASAIKE MISNETIAEA PKDCGDSAVN WESGKRLFQY LKSRNITGET GQVAFDDNGD
RIYAGYDVIN IREQQKKHVV GKFSYDSMRA KMRMRINDSE IIWPGKQRRK PEGIMIPTHL
KLLTIEEKPF VYVRRMGDDE FRCEPDERPC PLFNNSDATA NEFCCRGYCI DLLIELSKRI
NFTYDLALSP DGQFGHYILR NSTGAMTLRK EWTGLIGELV NERADMIVAP LTINPERAEY
IEFSKPFKYQ GITILEKKPS RSSTLVSFLQ PFSNTLWILV MVSVHVVALV LYLLDRFSPF
GRFKLSHSDS NEEKALNLSS AVWFAWGVLL NSGIGEGTPR SFSARVLGMV WAGFAMIIVA
SYTANLAAFL VLERPKTKLS GINDARLRNT MENLTCATVK GSSVDMYFRR QVELSNMYRT
MEANNYATAE QAIQDVKKGK LMAFIWDSSR LEYEASKDCE LVTAGELFGR SGYGIGLQKG
SPWTDAVTLA ILEFHESGFM EKLDKQWIFH GHVQQNCELF EKTPNTLGLK NMAGVFILVG
VGIAGGVGLI IIEVIYKKHQ VKKQKRLDIA RHAADKWRGT IEKRKTIRAS LAMQRQYNVG
LNSTHAPGTI SLAVDKRRYP RLGQRLGPER AWPGDAADVL RIRRPYELGK PGQSPKVIAT
NQPGMPMPML GKTRPQQSVL PPRYSPGYTS DVSHLVV
